Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:3.2.1.31 (beta-glucuronidase)
 7,680 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

"Capacitase," a product combining beta-amylase and beta-glucuronidase, was compatible with survival of bull spermatozoa frozen in whole milk-glycerol extender at final concentrations per ml of 0, 5, 10, and 20 mug of beta-amylase combined with 0, 75, 150, and 300 units of beta-glucuronidase, respectively. Bull semen was frozen in whole milk-glycerol extender containing the three lower concentrations of enzymes tested in the previous trial and used to inseminate 9057 first-service cows within 4 mo of freezing. The 60- to 90-day percent nonreturns were 74.6, 75.6, and 75.0. The same treatments plus a fourth one containing 10 mug of catalase per ml were fertility tested in another trial. Insemination of 16,842 cows resulted in 75.6, 74.1, 74.6, and 74.2% nonreturns. In this trial semen was held immersed in liquid nitrogen and distributed for immediate use each mo for 6 mo. There was no change in fertility during 6 mo of continuous storage at --196 C. Under the conditions tested neither catalase nor beta-amylase with beta-glucuronidase enhanced fertility of frozen bull semen.
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PMID:Fertility of bull semen frozen with beta-amylase, beta-glucuronidase, and catalase. 99 19

When rabbit sperm were pretreated with media of high ionic strength (380 mOsM), which had previously been shown to facilitate removal of sperm-bound seminal plasma components, and subsequently treated with follicular fluid the acrosome reaction was completed rapidly. Treatment of the sperm with follicular fluid alone yielded a greatly decreased rate of acrosome reaction completion, and treatment with the high-ionic strength medium alone caused no visible alteration to the sperm. These results suggest that removal of the sperm-bound seminal plasma components destabilizes the acrosome and prepares it to undergo the acrosome reaction. This destabilization is virtually completed after a 5-minute preincubation of the sperm in high-ionic strength media. Direct comparison of epididymal and ejaculated sperm indicated that epididymal sperm acrosomes were apparently in the same stabilized condition as ejaculated sperm. The effect of the pretreatment by high-ionic strength media could be partially mimicked by pretreatment of sperm with alpha- or beta-amylase or neuraminidase but not by beta-glucuronidase, lipase, pronase, or trypsin. Comparison of the ability of bovine follicular fluid, rabbit follicular fluid, and rabbit serum to induce the rabbit acrosome reaction showed that bovine follicular fluid was 3 to 4 times more effective than rabbit follicular fluid and that rabbit serum was totally ineffective in producing the acrosome reaction. The data support a physiologic role for follicular fluids in the process of fertilization and indicate that removal of sperm-bound seminal plasma components is a prerequisite to efficient induction of the acrosome reaction.
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PMID:Removal of sperm-bound seminal plasma components as a prerequisite to induction of the rabbit acrosome reaction. 124 42

Previous studies have shown that bovine retinas incubated with [3H]galactose incorporated it, unmodified, into large molecules. Light and electron microscope autoradiography showed a significant proportion of the label to be in cone inner segments, and pulse-chase studies showed it was subsequently transported to the synaptic pedicles. In this report, evidence is presented to show that the galactose-labelled macromolecules are resistant to hydrolysis by proteolytic enzymes, testicular hyaluronidase, chondroitinase ABC, beta-glucosidase and beta-glucuronidase, but are readily degraded by alpha-amylase and beta-galactosidase, and to a lesser extent by beta-amylase. Treatment with alpha-amylase also leads to specific removal of radioactivity from cone inner segments and pedicles, as judged by light-microscopic autoradiography. These studies appear to indicate that the cone-specific galactose label is in glycogen or glycogen-like molecules.
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PMID:D-[3H]galactose incorporation into glycogen in retinal cone cells. 231 72

M-GTFI, originally screened as an inhibitor of Streptococcus mutans glucosyltransferase, strongly inhibited alpha-glucosidase, in a non-competitive manner especially when the synthetic substrate p-nitrophenyl-alpha-D-glucopyranoside was used. It also inhibited beta-glucosidase, beta-amylase and, to a lesser extent, beta-glucuronidase. The inhibitor was stable in neutral and alkaline pH ranges and dependency of the inhibition on pH and temperature was not observed. Some proteinases and polysaccharides-hydrolyzing enzymes as well as human saliva did not inactivate the inhibitor. There was a correlation between the release of sulfate anions from the inhibitor molecule on incubation with HCl (0.2 N) at 100 degrees C and loss of inhibitory properties of the molecule. It is suggested that the presence of sulfate ester linkages in the inhibitor molecule play an important role in the inhibition process.
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PMID:Characteristics of M-GTFI, a new inhibitor of Streptococcus mutans glucosyltransferase. 297 50

The levels of beta-amylase activity and of the mRNA for beta-amylase in rosette leaves of Arabidopsis thaliana (L.) Heynh. increased significantly, with the concomitant accumulation of starch, when whole plants or excised mature leaves were supplied with sucrose. A supply of glucose or fructose, but not of mannitol or sorbitol, to plants also induced the expression of the gene for beta-amylase, and the induction occurred not only in rosette leaves but also in roots, stems, and bracts. These results suggest that the gene for beta-amylase of Arabidopsis is subject to regulation by a carbohydrate metabolic signal, and expression of the gene in various tissues may be regulated by the carbon partitioning and sink-source interactions in the whole plant. The sugar-inducible expression of the gene in Arabidopsis was severely repressed in the absence of light. The sugar-inducible expression in the light was not inhibited by 3(3,4-dichlorophenyl)-1,1-dimethylurea or by chloramphenicol, but it was inhibited by cycloheximide. These results suggest that a light-induced signal and de novo synthesis of proteins in the cytoplasm are involved in the regulation. A fusion gene composed of the 5' upstream region of the gene for beta-amylase from Arabidopsis and the coding sequence of beta-glucuronidase showed the sugar-inducible expression in a light-dependent manner in rosette leaves of transgenic Arabidopsis.
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PMID:Sugar-inducible expression of a gene for beta-amylase in Arabidopsis thaliana. 771 46

Genetic studies in Arabidopsis thaliana have shown that two members of the beta-amylase (BAM) family BAM3 and BAM4 are required for leaf starch breakdown at night. Both are plastid proteins and while BAM3 encodes an active BAM, BAM4 is not an active alpha-1,4-glucan hydrolase. To gain further insight into the possible function of BAM4 we constructed reporter genes using promoters for both BAM3 and BAM4 genes, driving beta-glucuronidase (GUS) and luciferase (LUC) expression in transgenic Arabidopsis plants. Both promoters directed expression in vascular tissue throughout the plant including cotyledons, leaves, petioles, stems, petals, siliques and roots. Tissue sections showed expression to be focused in phloem cells in stem and petiole. The BAM3 promoter was also expressed strongly throughout the photosynthetic tissues of leaves, sepals and siliques, whereas the BAM4 promoter was not. Conversely, the BAM4 promoter was active in root tip but the BAM3 promoter was not. To confirm these expression patterns and to compare with expression of other starch genes we carried-out RT-PCR analysis on RNA from vascular (replum) and non-vascular (valve) tissues of siliques. This confirmed that BAM4 expression together with RAM1 (BAM5) and GWD2 genes is stronger in the replum than the valve, whereas BAM3 is strong in both tissues. These results show that even though BAM3 and BAM4 genes apparently interact genetically in leaf starch metabolism, BAM4 is preferentially expressed in non-photosynthetic vascular tissue, so revealing a potentially greater level of complexity in the control of starch breakdown than had previously been recognised.
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PMID:The gene encoding the catalytically inactive beta-amylase BAM4 involved in starch breakdown in Arabidopsis leaves is expressed preferentially in vascular tissues in source and sink organs. 2015 46